Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Wolfgang Doster"'
Nanosecond structural dynamics of intrinsically disordered β-casein micelles by neutron spectroscopy
Autor:
Joachim Wuttke, Olaf Holderer, Wolfgang Doster, Marie-Sousai Appavou, Tobias E. Schrader, Michaela Zamponi, Dieter Richter, Hiroshi Nakagawa
Publikováno v:
Biophys J
β-casein undergoes a reversible endothermic self-association, forming protein micelles of limited size. In its functional state, a single β-casein monomer is unfolded, which creates a high structural flexibility, supposed to play a major role in pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df6902f54f46a251716fa8e4fe4a659d
https://pubmed.ncbi.nlm.nih.gov/34717964
https://pubmed.ncbi.nlm.nih.gov/34717964
Autor:
Wolfgang Doster
Publikováno v:
International Journal of Molecular and Theoretical Physics. 2:1-14
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad3c71132710b1b52d1dd919e5952409
https://doi.org/10.15226/2576-4934/2/1/00112
https://doi.org/10.15226/2576-4934/2/1/00112
Autor:
Wolfgang Doster
Publikováno v:
Proceedings of the National Academy of Sciences. 116:8649-8650
In PNAS, Kneller (1) suggests a quantum-theoretical justification of the “Frauenfelder energy landscape model” of protein dynamics applied to quasielastic neutron scattering (QENS) (2, 3). The diffusion-broadened QENS spectrum, centered at ω = 0
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::651feb67844443691bbf9ef68bf797cd
https://doi.org/10.1073/pnas.1821562116
https://doi.org/10.1073/pnas.1821562116
Publikováno v:
The Journal of Physical Chemistry B. 115:2349-2359
Caseins form heterogeneous micelles composed of three types of disordered protein chains (R, β, κ), which include protein-bound calcium phosphate particles. We probe the stability limits of themicelle by applying hydrostatic pressure. The resulting
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c9fc15048967662e63885881cc7828c
https://doi.org/10.1021/jp107622d
https://doi.org/10.1021/jp107622d
Publikováno v:
European Biophysics Journal. 40:705-714
Pressure is a ubiquitous physical parameter in life and is commonly used in the life sciences to study new protein folding pathways or association-dissociation phenomena. In this paper, an investigation of the influence of pressure on hemoglobin, a m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29f641c4745a57c55108482dede7ae80
https://doi.org/10.1007/s00249-011-0678-3
https://doi.org/10.1007/s00249-011-0678-3
Autor:
Wolfgang Doster
Publikováno v:
Journal of Non-Crystalline Solids. 357:622-628
The “protein dynamical transition” (PDT) characterizes the abrupt loss of structural flexibility at a particular temperature and time scale in response to the glass transition of protein hydration water. The water-coupled structural degrees of fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0fe2ddc61369f2bb7ff0cc82844c06ac
https://doi.org/10.1016/j.jnoncrysol.2010.08.002
https://doi.org/10.1016/j.jnoncrysol.2010.08.002
Autor:
Wolfgang Doster
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804:3-14
The protein dynamical transition and its connection with the liquid-glass transition (GT) of hydration water and aqueous solvents are reviewed. The protein solvation shell exhibits a regular glass transition, characterized by steps in the specific he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14dc45fc20af2ec23ffea6eb7890044c
https://doi.org/10.1016/j.bbapap.2009.06.019
https://doi.org/10.1016/j.bbapap.2009.06.019
Publikováno v:
European Biophysics Journal. 37:573-582
Casein proteins belong to the class of natively disordered proteins. The existence of disordered biologically active proteins questions the assumption that a well-folded structure is required for function. A hypothesis generally put forward is that t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f72cf8700f306f410710293e937cd0e
https://doi.org/10.1007/s00249-008-0266-3
https://doi.org/10.1007/s00249-008-0266-3
Publikováno v:
Biophysical journal 93, 960-968 (2007). doi:10.1529/biophysj.107.106385
The structure of thin casein films prepared with spin-coating is investigated as a function of the calcium concentration. Grazing incidence small-angle x-ray scattering and atomic force microscopy are used to probe the micelle structure. For comparis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::844b8af4af75598f7dafa143ea4937a9
Autor:
Wolfgang Doster
Publikováno v:
Physica B: Condensed Matter. :831-834
A moment analysis of the self-intermediate scattering function is used to reconstruct the distribution of structural displacements in the small protein myoglobin as a function of time, temperature and environment. Model-independent information is obt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f31a9d7b85341e26b4ad8fbc970869c1
https://doi.org/10.1016/j.physb.2006.05.117
https://doi.org/10.1016/j.physb.2006.05.117